Glioma cell activation by Alzheimer's peptide Abeta1-42, alpha1-antichymotrypsin, and their mixture.
(2002) In Cellular and Molecular Life Sciences 59(10). p.43-1734- Abstract
- We compared the effects of Alzheimer’s peptide
(Ab1–42), a1-antichymotrypsin (ACT) and an ACT/Ab1–42
mixture on human glioma DK-MG cells. The solution of
Ab (5 mM) formed by 2-h incubation at room temperature
induced tumour necrosis factor-a (TNF-a) and interleukin
(IL)-6 levels by 55 and 45%, respectively, and increased
gelatinase B activity by 67%, while exposure of
cells to the ACT/Ab1–42 mixture (1:10 molar ratio ACT:
Ab1–42) under the same experimental conditions showed
no effect on IL-6 levels or gelatinase B activity, but
strongly induced TNF-a (by 190%), compared to the con-
CMLS, Cell. Mol. Life Sci. 59 (2002) 1734–1743
... (More) - We compared the effects of Alzheimer’s peptide
(Ab1–42), a1-antichymotrypsin (ACT) and an ACT/Ab1–42
mixture on human glioma DK-MG cells. The solution of
Ab (5 mM) formed by 2-h incubation at room temperature
induced tumour necrosis factor-a (TNF-a) and interleukin
(IL)-6 levels by 55 and 45%, respectively, and increased
gelatinase B activity by 67%, while exposure of
cells to the ACT/Ab1–42 mixture (1:10 molar ratio ACT:
Ab1–42) under the same experimental conditions showed
no effect on IL-6 levels or gelatinase B activity, but
strongly induced TNF-a (by 190%), compared to the con-
CMLS, Cell. Mol. Life Sci. 59 (2002) 1734–1743
1420-682X/02/101734-11
© Birkhäuser Verlag, Basel, 2002 CMLS Cellular and Molecular Life Sciences
trols. Stimulation of the cells with Ab1–42 alone, but not
with ACT, increased by about 20% low-density lipoprotein
(LDL) uptake and mRNA levels for LDL receptor and
HMG-CoA reductase, while the ACT/Ab1–42 mixture significantly
increased LDL uptake (by 50%), up-regulated
mRNA levels for LDL receptor and HMG-CoA reductase
by 48 and 63%, respectively, and increased lipid accumulation
by about 20-fold. These data suggest a possible new
role for Ab in Alzheimer’s disease through its interaction
with the inflammatory reactant, ACT. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/114646
- author
- Sun, Yongxin LU ; Wright, H T and Janciauskiene, Sabina LU
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Kinetics, Peptide Fragments: chemical synthesis, Human, Interleukin-6: genetics, DNA Primers, DNA, Neoplastic: drug effects, Glioma: physiopathology, Amyloid beta-Protein: pharmacology, Base Sequence, Amyloid beta-Protein: chemical synthesis, Gene Expression Regulation, Neoplasm: biosynthesis, Gelatinase B: metabolism, Peptide Fragments: pharmacology, RNA, Messenger: genetics, Reverse Transcriptase Polymerase Chain Reaction, Support, Non-U.S. Gov't, Thymidine: metabolism, Transcription, Genetic: drug effects, Tumor Cells, Cultured, Tumor Necrosis Factor: genetics, alpha 1-Antichymotrypsin: pharmacology
- in
- Cellular and Molecular Life Sciences
- volume
- 59
- issue
- 10
- pages
- 43 - 1734
- publisher
- Birkhäuser Verlag
- external identifiers
-
- scopus:0036809846
- ISSN
- 1420-9071
- DOI
- 10.1007/PL00012501
- language
- English
- LU publication?
- yes
- id
- 18a24388-07ac-40da-8a41-332b2ccc3b74 (old id 114646)
- date added to LUP
- 2016-04-01 16:49:44
- date last changed
- 2022-04-23 00:49:38
@article{18a24388-07ac-40da-8a41-332b2ccc3b74,
abstract = {{We compared the effects of Alzheimer’s peptide<br/><br>
(Ab1–42), a1-antichymotrypsin (ACT) and an ACT/Ab1–42<br/><br>
mixture on human glioma DK-MG cells. The solution of<br/><br>
Ab (5 mM) formed by 2-h incubation at room temperature<br/><br>
induced tumour necrosis factor-a (TNF-a) and interleukin<br/><br>
(IL)-6 levels by 55 and 45%, respectively, and increased<br/><br>
gelatinase B activity by 67%, while exposure of<br/><br>
cells to the ACT/Ab1–42 mixture (1:10 molar ratio ACT:<br/><br>
Ab1–42) under the same experimental conditions showed<br/><br>
no effect on IL-6 levels or gelatinase B activity, but<br/><br>
strongly induced TNF-a (by 190%), compared to the con-<br/><br>
CMLS, Cell. Mol. Life Sci. 59 (2002) 1734–1743<br/><br>
1420-682X/02/101734-11<br/><br>
© Birkhäuser Verlag, Basel, 2002 CMLS Cellular and Molecular Life Sciences<br/><br>
trols. Stimulation of the cells with Ab1–42 alone, but not<br/><br>
with ACT, increased by about 20% low-density lipoprotein<br/><br>
(LDL) uptake and mRNA levels for LDL receptor and<br/><br>
HMG-CoA reductase, while the ACT/Ab1–42 mixture significantly<br/><br>
increased LDL uptake (by 50%), up-regulated<br/><br>
mRNA levels for LDL receptor and HMG-CoA reductase<br/><br>
by 48 and 63%, respectively, and increased lipid accumulation<br/><br>
by about 20-fold. These data suggest a possible new<br/><br>
role for Ab in Alzheimer’s disease through its interaction<br/><br>
with the inflammatory reactant, ACT.}},
author = {{Sun, Yongxin and Wright, H T and Janciauskiene, Sabina}},
issn = {{1420-9071}},
keywords = {{Kinetics; Peptide Fragments: chemical synthesis; Human; Interleukin-6: genetics; DNA Primers; DNA; Neoplastic: drug effects; Glioma: physiopathology; Amyloid beta-Protein: pharmacology; Base Sequence; Amyloid beta-Protein: chemical synthesis; Gene Expression Regulation; Neoplasm: biosynthesis; Gelatinase B: metabolism; Peptide Fragments: pharmacology; RNA; Messenger: genetics; Reverse Transcriptase Polymerase Chain Reaction; Support; Non-U.S. Gov't; Thymidine: metabolism; Transcription; Genetic: drug effects; Tumor Cells; Cultured; Tumor Necrosis Factor: genetics; alpha 1-Antichymotrypsin: pharmacology}},
language = {{eng}},
number = {{10}},
pages = {{43--1734}},
publisher = {{Birkhäuser Verlag}},
series = {{Cellular and Molecular Life Sciences}},
title = {{Glioma cell activation by Alzheimer's peptide Abeta1-42, alpha1-antichymotrypsin, and their mixture.}},
url = {{http://dx.doi.org/10.1007/PL00012501}},
doi = {{10.1007/PL00012501}},
volume = {{59}},
year = {{2002}},
}